BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19408

Title: Conformation and dynamics of the periplasmic membrane-protein chaperone complexes OmpX Skp and tOmpA Skp   PubMed: 24077225

Deposition date: 2013-08-03 Original release date: 2013-09-10

Authors: Burmann, Bjoern; Wang, Congwei; Hiller, Sebastian

Citation: Burmann, Bjoern; Wang, Congwei; Hiller, Sebastian. "Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp"  Nat. Struct. Mol. Biol. 20, 1265-1272 (2013).

Assembly members:
Escherichia_Coli_Skp, polymer, 234 residues, Formula weight is not available
Escherichia_Coli_OmpX, polymer, 150 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28B-Skp

Entity Sequences (FASTA):
Escherichia_Coli_Skp: MGSSHHHHHHSSGLVPRGSH MADKIAIVNMGSLFQQVAQK TGVSNTLENEFKGRASELQR METDLQAKMKKLQSMKAGSD RTKLEKDVMAQRQTFAQKAQ AFEQDRARRSNEERGKLVTR IQTAVKSVANSQDIDLVVDA NAVAYNSSDVKDITADVLKQ VKIYGVVGVGYGKFQQTENQ GLNRTASNSDYGFSYGAGMQ FNPIENVALDFSYEQSRIRN VDVGTWIAGVGYRF
Escherichia_Coli_OmpX: MATSTVTGGYAQSDMQGVMN KTNGFNLKYRYEQDNNPLGV IGSFTYTEKDRTENGSYNKG QYYGITAGPAYRLNDWASIY GVVGVGYGKFQQTENQGLNR TASNSDYGFSYGAGMQFNPI ENVALDFSYEQSRIRNVDVG TWIAGVGYRF

Data sets:
Data typeCount
13C chemical shifts283
15N chemical shifts149
1H chemical shifts149

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Skp, chain 11
2Skp, chain 21
3Skp, chain 31
4OmpX2

Entities:

Entity 1, Skp, chain 1 234 residues - Formula weight is not available

native processed E. coli SKP (residues 21 - 161) hexahistidin-tag and Thrombin cleavage site (coming from pET28b)

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METALAASPLYSILEALAILEVALASNMET
4   GLYSERLEUPHEGLNGLNVALALAGLNLYS
5   THRGLYVALSERASNTHRLEUGLUASNGLU
6   PHELYSGLYARGALASERGLULEUGLNARG
7   METGLUTHRASPLEUGLNALALYSMETLYS
8   LYSLEUGLNSERMETLYSALAGLYSERASP
9   ARGTHRLYSLEUGLULYSASPVALMETALA
10   GLNARGGLNTHRPHEALAGLNLYSALAGLN
11   ALAPHEGLUGLNASPARGALAARGARGSER
12   ASNGLUGLUARGGLYLYSLEUVALTHRARG
13   ILEGLNTHRALAVALLYSSERVALALAASN
14   SERGLNASPILEASPLEUVALVALASPALA
15   ASNALAVALALATYRASNSERSERASPVAL
16   LYSASPILETHRALAASPVALLEULYSGLN
17   VALLYSILETYRGLYVALVALGLYVALGLY
18   TYRGLYLYSPHEGLNGLNTHRGLUASNGLN
19   GLYLEUASNARGTHRALASERASNSERASP
20   TYRGLYPHESERTYRGLYALAGLYMETGLN
21   PHEASNPROILEGLUASNVALALALEUASP
22   PHESERTYRGLUGLNSERARGILEARGASN
23   VALASPVALGLYTHRTRPILEALAGLYVAL
24   GLYTYRARGPHE

Entity 2, OmpX 150 residues - Formula weight is not available

native processed E. coli OmpX (rseidues 24 - 172) + initiator methionine

1   METALATHRSERTHRVALTHRGLYGLYTYR
2   ALAGLNSERASPMETGLNGLYVALMETASN
3   LYSTHRASNGLYPHEASNLEULYSTYRARG
4   TYRGLUGLNASPASNASNPROLEUGLYVAL
5   ILEGLYSERPHETHRTYRTHRGLULYSASP
6   ARGTHRGLUASNGLYSERTYRASNLYSGLY
7   GLNTYRTYRGLYILETHRALAGLYPROALA
8   TYRARGLEUASNASPTRPALASERILETYR
9   GLYVALVALGLYVALGLYTYRGLYLYSPHE
10   GLNGLNTHRGLUASNGLNGLYLEUASNARG
11   THRALASERASNSERASPTYRGLYPHESER
12   TYRGLYALAGLYMETGLNPHEASNPROILE
13   GLUASNVALALALEUASPPHESERTYRGLU
14   GLNSERARGILEARGASNVALASPVALGLY
15   THRTRPILEALAGLYVALGLYTYRARGPHE

Samples:

sample_1: Escherichia Coli OmpX, [U-100% 2H], 0.2 – 0.35 mM; Escherichia Coli Skp (trimer), [U-13C; U-15N; U-2H], 0.6 – 1.05 mM; H2O 95%; D2O 5%; MES 25 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 0.150 M; pH: 6.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bartels et al., Bruker Biospin, Guntert, Keller and Wuthrich - chemical shift assignment, collection, data analysis, processing

NMR spectrometers:

  • Bruker AscendII 700 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UNP P0AEU7 P25253
BMRB 19407 19409 19730 19733
PDB
EMBL CDL25894
GB ADN44803 AFG39053 EDZ78162 EID69435 EMV37114
REF WP_001387023 WP_024201252 WP_050877050 WP_052985403 WP_052989315
AlphaFold P11457 P25253

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts